Evaluation of aminoglycoside and carbapenem resistance in a collection of drug-resistant pseudomonas aeruginosa clinical isolates

Selina Y.L. Holbrook, Sylvie Garneau-Tsodikova

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22 Scopus citations


Pseudomonas aeruginosa, a Gram-negative bacterium, is a member of the ESKAPE pathogens and one of the leading causes of healthcare-associated infections worldwide. Aminoglycosides (AGs) are recognized for their efficacy against P. aeruginosa. The most common resistance mechanism against AGs is the acquisition of AG-modifying enzymes (AMEs) by the bacteria, including AG N-acetyltransferases (AACs), AG O-phosphotransferases (APHs), and AG O-nucleotidyltransferases (ANTs). In this study, we obtained 122 multidrug-resistant P. aeruginosa clinical isolates and evaluated the antibacterial effects of six AGs and two carbapenems alone against all clinical isolates, and in combination against eight selected strains. We further probed for four representatives of the most common AME genes [aac(6′)-Ib, aac(3)-IV, ant(2»)-Ia, and aph(3′)-Ia] by polymerase chain reaction (PCR) and compared the AME patterns of these 122 clinical isolates to their antibiotic resistance profile. Among the diverse antibiotics resistance profile displayed by these clinical isolates, we found correlations between the resistance to various AGs as well as between the resistance to one AG and the resistance to carbapenems. PCR results revealed that the presence of aac(6′)-Ib renders these isolates more resistant to a variety of antibiotics. The correlation between resistance to various AGs and carbapenems partially reflects the complex resistance strategies adapted in these pathogens and encourages the development of strategic treatment for each P. aeruginosa infection by considering the genetic information of each isolated bacteria.

Original languageEnglish
Pages (from-to)1020-1030
Number of pages11
JournalMicrobial Drug Resistance
Issue number7
StatePublished - Sep 2018

Bibliographical note

Funding Information:
This work was supported by NIH grant AI090048 (to S.G.-T.). S.Y.L.H. was in part supported by a University of Kentucky Presidential Fellowship. We thank Prof. David S. Burgess for sharing with us the clinical isolates that we used in this study.

Publisher Copyright:
© 2018 Mary Ann Liebert, Inc.


  • ESKAPE pathogens
  • aminoglycoside-modifying enzymes (AMEs)
  • drug combination
  • resistance patterns

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Pharmacology
  • Microbiology (medical)


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